Recombinant expression analysis of natural and synthetic bovine alpha-casein in Escherichia coli
UNSPECIFIED. (2000) Recombinant expression analysis of natural and synthetic bovine alpha-casein in Escherichia coli. APPLIED MICROBIOLOGY AND BIOTECHNOLOGY, 54 (5). pp. 671-676. ISSN 0175-7598Full text not available from this repository.
As a prelude to developing a yeast-based fermentation process for the production of phenylalanine-free alpha-casein as a foodstuff for patients suffering from phenylketonuria, we cloned the gene encoding bovine alpha-casein. We synthesised a modified gene sequence encoding the same, but devoid of phenylalanine codons and with a codon bias similar to that of naturally occurring highly expressed genes in Saccharomyces cerevisiae. The results show that both gene sequences are readily expressed in Escherichia coli when cloned in an E. coli bacteriophage T7 promoter-driven plasmid vector. In this host, the natural and synthetic casein proteins were produced at levels equating to 18.0% and 7.6% of the cell's soluble protein, respectively.
|Item Type:||Journal Article|
|Subjects:||T Technology > TP Chemical technology|
|Journal or Publication Title:||APPLIED MICROBIOLOGY AND BIOTECHNOLOGY|
|Official Date:||November 2000|
|Number of Pages:||6|
|Page Range:||pp. 671-676|
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